| pubmed-article:11792827 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11792827 | lifeskim:mentions | umls-concept:C0014239 | lld:lifeskim |
| pubmed-article:11792827 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:11792827 | lifeskim:mentions | umls-concept:C0065702 | lld:lifeskim |
| pubmed-article:11792827 | lifeskim:mentions | umls-concept:C1416994 | lld:lifeskim |
| pubmed-article:11792827 | pubmed:issue | Pt 24 | lld:pubmed |
| pubmed-article:11792827 | pubmed:dateCreated | 2002-1-16 | lld:pubmed |
| pubmed-article:11792827 | pubmed:abstractText | The alpha1,2-mannosidase Mns1p involved in the N-glycosidic pathway in Saccharomyces cerevisiae is a type II membrane protein of the endoplasmic reticulum. The localization of Mns1p depends on retrieval from the Golgi through a mechanism that involves Rer1p. A chimera consisting of the transmembrane domain of Mns1p fused to the catalytic domain of the Golgi alpha1,2-mannosyltransferase Kre2p was localized in the endoplasmic reticulum of Deltapep4 cells and in the vacuoles of rer1/Deltapep4 by indirect immunofluorescence. The split-ubiquitin system was used to determine if there is an interaction between Mns1p and Rer1p in vivo. Co-expression of NubG-Mns1p and Rer1p-Cub-protein A-lexA-VP16 in L40 yeast cells resulted in cleavage of the reporter molecule, protein A-lexA-VP16, detected by western blot analysis and by expression of beta-galactosidase activity. Sec12p, another endoplasmic reticulum protein that depends on Rer1p for its localization, also interacted with Rer1p using the split-ubiquitin assay, whereas the endoplasmic reticulum protein Ost1p showed no interaction. A weak interaction was observed between Alg5p and Rer1p. These results demonstrate that the transmembrane domain of Mns1p is sufficient for Rer1p-dependent endoplasmic reticulum localization and that Mns1p and Rer1p interact. Furthermore, the split-ubiquitin system demonstrates that the C-terminal of Rer1p is in the cytosol. | lld:pubmed |
| pubmed-article:11792827 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11792827 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11792827 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11792827 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11792827 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:11792827 | pubmed:issn | 0021-9533 | lld:pubmed |
| pubmed-article:11792827 | pubmed:author | pubmed-author:HerscovicsAA | lld:pubmed |
| pubmed-article:11792827 | pubmed:author | pubmed-author:MassaadM JMJ | lld:pubmed |
| pubmed-article:11792827 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11792827 | pubmed:volume | 114 | lld:pubmed |
| pubmed-article:11792827 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11792827 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11792827 | pubmed:pagination | 4629-35 | lld:pubmed |
| pubmed-article:11792827 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:11792827 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11792827 | pubmed:articleTitle | Interaction of the endoplasmic reticulum alpha 1,2-mannosidase Mns1p with Rer1p using the split-ubiquitin system. | lld:pubmed |
| pubmed-article:11792827 | pubmed:affiliation | McGill Cancer Centre, McGill University, Montréal, Québec H3G 1Y6, Canada. | lld:pubmed |
| pubmed-article:11792827 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11792827 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11792827 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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